ID I9UX85_9BACE Unreviewed; 1051 AA.
AC I9UX85;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU361154};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU361154};
DE AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230, ECO:0000256|RuleBase:RU361154};
GN ORFNames=HMPREF1074_01018 {ECO:0000313|EMBL:EIY87441.1};
OS Bacteroides xylanisolvens CL03T12C04.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=997892 {ECO:0000313|EMBL:EIY87441.1, ECO:0000313|Proteomes:UP000003566};
RN [1] {ECO:0000313|EMBL:EIY87441.1, ECO:0000313|Proteomes:UP000003566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL03T12C04 {ECO:0000313|EMBL:EIY87441.1,
RC ECO:0000313|Proteomes:UP000003566};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Zitomersky N.L., Coyne M.J.,
RA Comstock L.E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Bacteroides xylanisolvens CL03T12C04.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC in beta-D-galactosides.; EC=3.2.1.23;
CC Evidence={ECO:0000256|ARBA:ARBA00001412,
CC ECO:0000256|RuleBase:RU361154};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EIY87441.1}.
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DR EMBL; AGXE01000006; EIY87441.1; -; Genomic_DNA.
DR AlphaFoldDB; I9UX85; -.
DR PATRIC; fig|997892.3.peg.1044; -.
DR HOGENOM; CLU_002346_0_2_10; -.
DR Proteomes; UP000003566; Unassembled WGS sequence.
DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR004199; B-gal_small/dom_5.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR023230; Glyco_hydro_2_CS.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR032312; LacZ_4.
DR PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR Pfam; PF02929; Bgal_small_N; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR Pfam; PF16353; LacZ_4; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1051
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003728418"
FT DOMAIN 769..1044
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1051 AA; 121730 MW; 53D8608FF5013738 CRC64;
MINRLFSTLL FLSCLFCGLS PTAKAQNNEW ENPTQYEWNK EKPHADFRLY ERADDAVNDN
PQKSPWQYSL NGTWKFVYAP SIAESIKDFY RTDLSDNDWD TIIVPSNWEI QGFGEPIIRN
IQYVFSPNPP YIDVDNPVGT YRRTFTVPQN WQGREVLLHF GSISGYARIY VNGQQVGMTK
ASKTPAEFNV TNYLKKGENL LAVQVYRWHD GSYMEDQDFW RLSGIERDVF LTAYPQTTIW
DFFLHAGLDD TYRHGQFRAT VDLRSFNTNA TLQKGTLTLD LKDAGGKTVL SAQKVYCISD
ISTTLTFEGT VRNVRKWSAE HPSLYDCILT LRSDGDKQQT VVAHKVGFRR IEIKNARLLV
NGVPTYIKGV NRHEHNDTLG HVQTREIIMN DLRLIKQLNM NAVRTSHYPN HPLFYQLCDQ
YGIYVVDEAN IETHGMGSVP YFKDTIPHPA YRPEWYAAHV DRITRMVERD KNHPCIIGWS
LGNECGNGIV FHDEYKRLKK YDPGRFVQFE QAWEDWNTDV VCPMYPNMWK ITEYRKSGKQ
RPFIMCEYAH AQGNSNGNFK DLWDIIYDSP NLQGGFIWDF MDQGFKVKTE PRDGRTYWTY
NGKMGSYKWL EDKKGELNTG TDGLISANGI PKPQAYEVKK VYQYIQFSAK DLGKGIISIK
NRYDFTNLDE YAFIWEIYKN GEKISTGDFN VDLIPHEEKE IRLSLPVIPE DGNEYFLNLY
AHTRVATDLV PAGYEVAREQ MQLNKSSFFT SLPPCSGKLS YETKDNILSF QSGGVSGKID
LKKGILFDYM INGEQPIKQY PEPAFWRAPI DNDFGNKMPT LAGVWRTAHV NRYVKKVTID
EQNEKGLSIR IDWILNDIQV PYMMEYLICN NGAIVVTGSI DLTGTKLPEL PRFGMRMELH
QPYENLVYYG RGPFENYIDR YSSSFIGRYE DKVENQFYWY TRPQETGNKT DVRWLSLLDS
EGQGVRITGL QPIAFSALHF SPEDLDPGLT RKLQHTIDIV PQKNIFLHVD LKQRGLGGDN
SWGMYPHNEY RLLDKKYTYS YMIELVKKNS D
//
